Nuclear magnetic resonance provides a nondestructive method for observing the local environment structure, dynamics, and thermodynamics of molecules. Recent developments in the basic cross polarization spectroscopy have made it possible to do high resolution nmr spectroscopy under conditions when it was formally impossible, namely the solid or semisolid state. This approach now provides virtually unlimited opportunity for examination of the critical regions of macromolecules, and in particular protein molecules in the solid state. This project will initially address exploratory aspects of this technique. It will investigate side chain motion in protein crystals, motion in protein powders, as a function of hydration, motion and structure in protein gels, structure and dynamics in frozen protein solutions. In addition it will explore the applicability of the method to macromolecular aggregates and particulate systems, and an investigation of macromolecules binding sites for metal ions with spin 1/2. Finally it will exploit specific isotope enrichment procedures for focusing on a particular region in a protein molecule such as the active site to obtain high resolution data as a function of the physical state of the protein.